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Stat91的单个磷酸化酪氨酸残基是γ干扰素激活基因所必需的。

A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma.

作者信息

Shuai K, Stark G R, Kerr I M, Darnell J E

机构信息

Rockefeller University, Laboratory of Molecular Cell Biology, New York, NY 10021.

出版信息

Science. 1993 Sep 24;261(5129):1744-6. doi: 10.1126/science.7690989.

Abstract

Interferon-gamma (IFN-gamma) stimulates transcription of specific genes by inducing tyrosine phosphorylation of a 91-kilodalton cytoplasmic protein (termed STAT for signal transducer and activator of transcription). Stat91 was phosphorylated on a single site (Tyr701), and phosphorylation of this site was required for nuclear translocation, DNA binding, and gene activation. Stat84, a differentially spliced product of the same gene that lacks the 38 carboxyl-terminal amino acids of Stat91, did not activate transcription, although it was phosphorylated and translocated to the nucleus and bound DNA. Thus, Stat91 mediates activation of transcription in response to IFN-gamma.

摘要

γ干扰素(IFN-γ)通过诱导一种91千道尔顿的细胞质蛋白(称为信号转导子和转录激活子,即STAT)的酪氨酸磷酸化来刺激特定基因的转录。Stat91在单个位点(Tyr701)上被磷酸化,该位点的磷酸化是核转位、DNA结合和基因激活所必需的。Stat84是同一基因的差异剪接产物,缺少Stat91的38个羧基末端氨基酸,虽然它被磷酸化并转位到细胞核且能结合DNA,但不能激活转录。因此,Stat91介导了对IFN-γ的转录激活反应。

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